JARID2 and AEBP2 regulate PRC2 in the presence of H2AK119ub1 and other histone modifications-Reference-Cited by-同舟云学术

JARID2 and AEBP2 regulate PRC2 in the presence of H2AK119ub1 and other histone modifications

Published:2021-01-22 Issue:6527 Volume:371 Page:
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Kasinath Vignesh¹^ORCID,Beck Curtis²^ORCID,Sauer Paul¹³^ORCID,Poepsel Simon⁴⁵^ORCID,Kosmatka Jennifer²^ORCID,Faini Marco⁶^ORCID,Toso Daniel¹,Aebersold Ruedi⁶⁷^ORCID,Nogales Eva¹²³⁸^ORCID

Affiliation:

1. QB3 Institute, Department of Molecular and Cell Biology, University of California, Berkeley, CA, USA.

2. Department of Molecular and Cellular Biology, University of California, Berkeley, CA, USA.

3. Howard Hughes Medical Institute, University of California, Berkeley, CA, USA.

4. University of Cologne, Center for Molecular Medicine Cologne (CMMC), Faculty of Medicine and University Hospital, Cologne, Germany.

5. Cologne Excellence Cluster for Cellular Stress Responses in Ageing-Associated Diseases (CECAD), University of Cologne, Cologne, Germany.

6. Department of Biology, Institute of Molecular Systems Biology, ETH Zürich, Zürich, Switzerland.

7. Faculty of Science, University of Zürich, Zürich, Switzerland.

8. Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA, USA.

Abstract

Cryo-EM uncovers polycomb interactions Polycomb family enzymes include the chromatin modifiers PRC1 and PRC2, which are involved in gene repression. Although the catalytic functions of these complexes are well known, their functional relationship is not. Kasinath et al. used cryo–electron microscopy (cryo-EM) to visualize the interactions between nucleosomes containing ubiquitinated histone H2A, the product of PRC1, and the PRC2-activating cofactors JARID2 and AEBP2, providing the molecular basis for PRC1-dependent recruitment of PRC2. They also show that JARID2 and AEBP2 partially overcome the inhibitory effect of PRC2 by two trimethyl lysine transcription marks on histones. This work suggests that PRC2 regulation involves an intricate interplay between PRC2 cofactors and histone posttranslational modifications. Science , this issue p. eabc3393

Funder

National Institute of General Medical Sciences

European Research Council

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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